• Title of article

    Antibody reactivity to the major fish allergen parvalbumin is determined by isoforms and impact of thermal processing

  • Author/Authors

    Saptarshi، نويسنده , , Shruti R. and Sharp، نويسنده , , Michael F. and Kamath، نويسنده , , Sandip D. and Lopata، نويسنده , , Andreas L.، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2014
  • Pages
    8
  • From page
    321
  • To page
    328
  • Abstract
    The EF-hand calcium binding protein, parvalbumin, is a major fish allergen. Detection of this allergen is often difficult due to its structural diversity among various fish species. The aim of this study was to evaluate the cross-reactivity of parvalbumin in a comprehensive range of bony and cartilaginous fish, from the Asia-Pacific region, and conduct a molecular analysis of this highly allergenic protein. Using the monoclonal anti-parvalbumin antibody PARV-19, we demonstrated the presence of monomeric and oligomeric parvalbumin in all fish analysed, except for gummy shark a cartilaginous fish. Heat processing of this allergen greatly affected its antibody reactivity. While heating caused a reduction in antibody reactivity to multimeric forms of parvalbumins for most bony fish, a complete loss of reactivity was observed for cartilaginous fish. Molecular analysis demonstrated that parvalbumin cross-reactivity, among fish species, is due to the molecular phylogenetic association of this major fish allergen.
  • Keywords
    Seafood , monoclonal antibody , allergen , parvalbumin , IgE epitopes , Asia-Pacific fish
  • Journal title
    Food Chemistry
  • Serial Year
    2014
  • Journal title
    Food Chemistry
  • Record number

    1976176